WORLD INTELLECTUAL PROPERTY ORGANIZATION
International Bureau
per
INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT)
(51) International Patent Classification 5
A21D 8/04
Al
(11) International Publication Number:
(43) International Publication Date:
WO 91/04669
18 April 1991 (18.04.91)
(21) International Application Number: PCT/DK90/00244
(22) International Filing Date : 26 September 1 990 (26.09.90)
(30) Priority data:
4745/89
27 September 1989 (27.09.89) DK
(71) Applicant (for all designated States except US): NOVO
NORDISK A/S [DK/DK]; Novo Alle, DK-2880 Bags-
vserd (DK).
(72) Inventor; and
(75) Inventor/Applicant (for US only) : OLESEN, Tine [DK/
DK]; Hagens Alle 57, DK-2900 Hellerup (DK).
(74) Agent: Patent Department; Novo Nordisk A/S, Novo Alle,
DK-2880 Bagsvaerd (DK).
(81) Designated States: AT (European patent), AU, BE (Euro-
pean patent), CA, CH (European patent), DE (Euro-
pean patent)*, DK (European patent), ES (European pa-
tent), FI, FR (European patent), GB (European patent),
IT (European patent), JP, LU (European patent), NL
(European patent), NO, SE (European patent), US.
Published
With international search report.
(54) Title: ANTISTALING PROCESS AND AGENT
(57) Abstract
The staling of leavened baked products such as bread is retarded by adding an enzyme with exoamylase activity to the
flour or dough used for producing the baked product in question.
* See back of page
DESIGNATIONS OF "DE"
Until further notice, any designation of "DE" in any international application
whose international filing date is prior to October 3, 1990, shall have effect in the
territory of the Federal Republic of Germany with the exception of the territory of the
former German Democratic Republic.
FOR THE PURPOSES OF INFORMATION ONLY
Codes used to identify States party to the PCT on the front pages of pamphlets publishing international
applications under the PCT.
AT
Austria
ES
Spain
MC
Monaco
AU
Australia
FI
Finland
MG
Madagascar
BB
Barbados
FR
France
ML
Mali
BE
Belgium
CA
Gabon
MR
Mauritania
BF
Burkina Fasso
GB
United Kingdom
MW
Malawi
BG
Bulgaria
GR
Greece
NL
Netherlands
BJ
Benin
Hll
Hungary
NO
Norway
BR
Brazil
IT
Italy
PL
Poland
CA
Canada
JP
Japan
RO
Romania
CF
Central African Republic
KP
Democratic People's Republic
SD
Sudan
CC
Congo
of Korea
SE
Sweden
CH
Switzerland
KR
Republic of Korea
SN
Senegal
CM
Cameroon
LI
Liechtenstein
su
Soviet Union
DE
Germany
LK
Sri Lanka
TD
Chad
DK
Denmark
LU
Luxembourg
TG
Togo
US
United States of America
WO 91/04669 PCT/DK90/00244
ANTISTALING PROCESS AND AGENT
FIELD OF INVENTION
The present invention relates to a process for retarding the
staling of bread and similar baked products, as well as an
5 agent for use in the process.
BACKGROUND OF THE INVENTION
Staling of baked products, principally bread, has been as-
cribed to certain properties of the starch component of flour.
Starch is essentially composed of amylose forming the core of
10 starch granules and amylopectin forming the outer "envelope" of
starch granules. Starch suspensions have been observed to
retrograde on standing to precipitate the amylose which, by
some, has been given as the explanation of the phenomenon of
staling. Others have explained staling of bread in terms of the
15 amylopectin chains in starch associating to cause a greater
rigidity of the bread crumb which is characteristic of stale
bread.
It is generally recognized to be of some commercial importance
to retard the staling of baked products so as to improve their
20 shelf-life. Retardation of the staling process may, for
instance, be brought about by the addition of monoglycerides
to dough. The antistaling effect of the monoglycerides may
partly be ascribed to their ability to bind water and partly
to the formation of monoglyceride-amylose complexes wherein
25 the long hydrocarbon chain penetrates into the cavity of the
amylose helix and thereby stabilise the helical structure to
prevent retrogradation.
Enzymatic retardation of staling by means of a-amylases has
also been described, vide for instance US 2,615,810 and US
30 3,026,205 as well as O. Silberstein, "Heat-Stable Bacterial
WO 91/04669
PCT/DK90/00244
2
Alpha-Amylase in Baking", Baker's Digest 38 (4), Aug. 1964, pp.
66-70 and 72. The use of a-amylase for retarding the staling of
bread has, however, not become widespread. The reason for this
is assumed to be that the medium-molecular weight branched
5 compounds, termed maltodextrins (with 20-100 glucose units in
the molecule) , generated through the hydrolytic action of a-
amylases have a sticky consistency in themselves resulting in
the formation of a sticky or gummy crumb, and consequently an
unacceptable mouthfeel, of the baked product if the a-amylase
10 is overdosed so that the maltodextrins are present in excessive
quantities .
It has previously been suggested to remedy the deleterious
effects of very large doses of a-amylase added to dough by
adding a debranching enzyme such as pullulanase, cf. US
15 4,654,216, the contents of which are incorporated herein by
reference. The theory behind the addition of a debranching
enzyme to obtain an antistaling effect while concomitantly
avoiding the risk of producing a gummy crumb in the resulting
bread is that by cleaving off the branched chains of the dex-
2 0 trins generated by a-amylase hydrolysis which cannot be de-
graded further by the a-amylase, the starch is converted to
oligosaccharides which do not cause gumminess.
SUMMARY OF THE INVENTION
The present invention represents a different approach to the
25 problem of crumb gumminess likely to result from the excessive
use of a-amylase for retarding the staling of bread. Thus, the
present invention relies on the use of an enzyme which is
capable of retarding the staling of baked products but which
does not hydrolyze starch into the above-mentioned branched
3 0 dextrins.
It has surprisingly been found that when the enzyme added to
dough used for producing baked products is an exoamylase, an
antistaling effect is obtained whereas the formation of a
WO 91/04669
PCT/DK90/00244
3
sticky or gummy crumb is substatially avoided except at very
high levels of the enzyme which also give rise to other del-
eterious effects likely to be discovered when the baked pro-
ducts are subjected to quality control.
5 It was also found that by using exoamylase enzymes one avoids
a certain softness and stickiness of the dough which is often
encountered when a-amylases, especially fungal a-amylases, are
used for antistaling, and especially if the a-amylase has been
overdosed, even if only to a mild degree.
10 Accordingly, the present invention relates to a process for
retarding the staling of leavened baked products, which pro-
cess comprises adding an enzyme with exoamylase activity to
flour or dough used for producing said baked products. In the
following, this enzyme is usually referred to as an "exo-
15 amylase".
In another aspect, the present invention relates to a baked
product produced by the present process.
It will often be advantageous to provide the exoamylase in
admixture with other ingredients commonly used to improve the
20 properties of baked products. These are commonly known as "pre-
mixes" and are employed not only in industrial bread-baking
plants/facilities, but also in retail bakeries where they are
usually supplied in admixture with flour.
Hence, in a further aspect, the present invention relates to
25 an agent for improving the quality of leavened, in particular
yeast leavened, baked products, which agent comprises an en-
zyme with exoamylase activity in liquid or substantially dry
form. For the present purpose, such an agent will be termed a
"bread improver" in the following description although it will
3 0 be understood that it may also be used for addition to other
types of leavened baked products such as rolls, certain kinds
of cakes, muffins, buns, etc.
WO 91/04669
PCT/DK90/00244
4
DETAILED DISCLOSURE OF THE INVENTION
Exoamylases are enzymes which hydrolyse (l->4) a-glucosidic
linkages in starch (and related polysaccharides) by removing
mono- or oligosaccharide units from the non-reducing ends of
5 the polysaccharide chains. The reducing groups liberated from
the polysaccharide molecule may be in the a- or B-configura-
tion. Examples of exoamylases which are useful for the present
purpose are 6-amylase (which releases maltose in the 6-
conf iguration) and maltogenic amylase (which releases maltose
10 in the a-conf iguration, but in contrast to a-amylases
predominantly produces maltotriose and maltotetraose and only
minor amounts of higher oligosaccharides) . The antistaling
effect of adding exoamylase to dough is currently believed to
be ascribable to the formation of sugars with a high water
15 retention capacity which makes the baked product in question
appear fresh (soft) for longer periods of time (e.g. glucose,
maltose, maltotriose and/or maltotetraose) , as well as to the
modification of the native starch which reduces the tendency to
retrogradation. Overdosing with the exoamylase resulting in
2 0 crumb stickiness is less likely to occur because the formation
of branched maltodextrins with 20-100 glucose units to which
the stickiness may be ascribed is, if not completely avoided,
at least significantly lower than when using a-amylase.
The use of amylase (primarily a-amylase) , invertase and poly-
25 saccharidase, as well as glucosidase (an exoamylase)) is sug-
gested in EP 136 158 and EP 13 6 159 for the preparation of
cookies with a moist crumb structure. Amylase is capable of
forming crystallization-resistant sugar, which is able to bind
water, from one or more ingredients in the dough resulting in
3 0 the aforementioned moist crumb when the dough is subsequently
baked. The cookies are indicated to be storage-stable.
It appears that the selection of the enzyme according to EP
136 158 and EP 136 159 is made with the object of obtaining a
WO 91/04669
PCT/DK90/00244
5
moist crumb structure due to the formation of water-binding
sugars from starch. With this end in view, pregelatinized
starch is added to the dough to facilitate enzymatic hydroly-
sis into various sugar species. It further appears that the
5 risk of obtaining a gummy crumb in the baked product through
addition of too large an amount of a-amylase is not a problem
to be avoided, but rather that moistness of the baked crumb is
the end result which the inventions disclosed in the above-
mentioned EP applications intend to achieve. In fact, a-
10 amylase which is known to produce crumb gumminess in leavened
bread even when added in relatively low quantities is the
preferred enzyme according to EP 13 6 159, the branched
maltodextrins produced by the a-amylase apparently providing
satisfactory moisture characteristics to the cookies produced.
15 contrary to this, the object of the present invention is to
avoid a sticky or gummy crumb in the baked product. The prin-
cipal difference between the baked products disclosed in the
EP applications and those produced by the present process re-
sides chiefly in the type of dough used to make the respect-
20 ive products. The products made by the present process are
leavened which implies that the gluten in the dough which is
composed of layers of protein "sheets" joined to bimolecular
layers of lipo- and phospholipoproteins is expanded by the
carbon dioxide produced by the leavening agent (e.g. yeast)
25 into a thin film which coagulates to a firm structure on
heating. Starch serves to make the structure firmer as, on
heating, it solidifies within the gluten structure. Thus, when
preparing leavened baked products including an amylase enzyme
to provide the antistaling effect, care must be taken to select
30 one which results in a hydrolysis product with a good water
retention capacity (e.g. maltose, maltotriose and/or
maltotetraose) and sufficient modification of the amylase and
amylopectin to retard retrogradation so as to provide a longer-
lasting softness of the baked product, without, however,
35 excessively affecting the structure of the native starch. This
seems to generate a hydrolysis product with a sticky consisten-
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6
cy (e.g. the branched maltodextrins with 20-100 glucose units
produced by a-amylase) which would tend to impair this struc-
ture.
Consistent with the explanation given above, a preferred exo-
5 amylase for use in the present process is one which exhibits
exoamylase activity at and above the gelation temperature of
starch (i.e. about 60-70 °C), as it has been found that the
retrogradation of starch and consequently the precipitation of
amylose responsible for staling takes place at this tem-
10 perature. Another reason is that starch hydrolysis is facili-
tated when the starch is gelatinized such that the swelling of
the starch granules caused by their uptake of liquid (water)
liberated by the coagulation of gluten loosens the normally
tight structure of the starch granules to make them more
15 accessible to enzyme activity. This leads to a hydrolysis of
the starch which is sufficient to retard retrogradation and to
form adequate amounts of sugar without excessively modifying
the native starch, resulting in an improved water retention.
Contrary to such a heat-stable exoamylase, cereal fi-amylases
2 0 inherently present in flour exhibit little starch hydrolytic
activity in the process of baking as they are inactive at the
gelation temperature of starch. It should be noted that the
exoamylases will be inactivated later in the baking process, at
temperatures above about 90 °C so that substantially no
25 residual exoamylase activity remains in the baked bread.
Preferred exoamylase enzymes are microbial exoamylases as these
are easier to produce on a large scale that exoamylases of, for
instance, plant origin. An example of a suitable exoamylase is
a maltogenic amylase producible by Bacillus strain NCIB 11837,
3 0 or one encoded by a DNA sequence derived from Bacillus strain
NCIB 11837 (the maltogenic amylase is disclosed in US 4,598,048
and US 4,604,355, the contents of which are incorporated herein
by reference) This maltogenic amylase is capable of hydrolyzing
1,4-a-glucosidic linkages in starch, partially hydrolyzed
35 starch and oligosaccharides (e.g. maltotriose) . Maltose units
WO 91/04669
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7
are removed from the non-reducing chain ends in a stepwise
manner. The maltose released is in the a-conf iguration. In the
US Patents mentioned above, the maltogenic amylase is indicated
to be useful for the production of maltose syrup of a high
5 purity. Another maltogenic amylase which may be. used in the
present process is a maltogenic fi-amylase producible by
Bacillus strain NCIB 11608 (disclosed in EP 234 858, the
contents of which are hereby incorporated by reference) .
For the present purpose, this maltogenic amylase may be added
10 to flour or dough in an amount of 0.1-10,000 MANU, preferably
1-5000 MANU, more preferably 5-2000 MANU, and most preferably
10-1000 MANU, per kg of flour. One MANU (Maltogenic Amylase
Novo Unit) may be defined as the amount of enzyme required to
release one nmol of maltose per minute at a concentration of 10
15 mg of maltotriose (Sigma M 8378) substrate per ml of 0.1 M
citrate buffer, pH 5.0 at 37 °C for 30 minutes.
The dough may be leavened in various ways such as by adding
sodium bicarbonate or the like or by adding a leaven (fer-
menting dough), but it is preferred to leaven the dough by
2 0 adding a suitable yeast culture such as a culture of Sacz
charomvces nerevisiae (baker's yeast). Any one of the commer-
cially available S^. cerevisiae strains may be employed.
The baked product is generally one made from, or at least
containing a certain amount of, wheat flour as such baked
25 products are more susceptible to staling than products made
from, for instance, rye flour due to their airier structure.
Thus, the baked product may be selected from the group con-
sisting of white bread, whole-meal bread, and bread prepared
from mixtures of wheat and rye flour. Of course rolls or the
3 0 like made from the same type of dough are also included in this
definition.
In the present process, the exoamylase enzyme may be added to
the dough in the form of a liquid, in particular a stabilized
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8
liquid, or it may be added to flour or dough as a substantially
dry powder or granulate. Granulates may be produced, e.g. as
disclosed in US 4,106,991 and US 4,661,452. Liquid enzyme
preparations may, for instance, be stabilized by adding a sugar
5 or sugar alcohol or lactic acid according to established
procedures. Other enzyme stablilizers are well-known in the
art.
In accordance with established practice in the baking art, one
or more other enzymes may be added to the flour or dough.
10 Examples of such enzymes are a-amylase (useful for providing
sugars fermentable by yeast although it should only be added in
limited quantities, for the reasons given above) , pentosanase
(useful for the partial hydrolysis of pentosans which in-
creases the extensibility of the dough) or a protease (useful
15 for gluten weakening, in particular when using hard wheat
flour) .
Also in accordance with established baking practice, one or
more emulsifiers may be added to the flour or dough.
Emulsifiers serve to improve dough extensibility and may also
2 0 be of some value for the consistency of the resulting bread,
making it easier to slice, as well as for its storage
stability, as explained above. Examples of suitable emulsifiers
are mono- or diglycerides, poly oxy ethylene stearates, diacetyl
tartaric acid esters of monoglycerides, sugar esters of fatty
25 acids, propylene glycol esters of fatty acids, polyglycerol
esters of fatty acids, lactic acid esters of monoglycerides,
acetic acid esters of monoglycerides, lecithin or
phospholipids .
When the bread improver of the invention is provided as a
3 0 substatially dry formulation, it will typically contain the
exoamylase in substantially dry form. The enzyme may thus be
in the form of a solid powder or granulate which may be pre-
pared in a manner known per se as indicated above. The term
"substantially dry formulation" should, in the present con-
WO 91/04669
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9
text, be understood to mean that the formulation should appear
as a dry and free-flowing powder and that the moisture content
of the bread improver formulation should not exceed about 15%,
and preferably not exceed about 10%. When the bread improver is
5 in the form of a semi-liquid preparation, the enzyme may also
be incorporated in liquid form.
Apart from the exoamylase, the bread improver of the invention
may typically comprise one or more components selected from the
group consisting of milk powder (providing crust colour),
10 gluten (to improve the gas retention power of weak flours) , an
emulsifier (such as one of those mentioned above) , granulated
fat (for dough softening and consistency of bread), an oxidant
(added to strengthen the gluten structure; e.g. ascorbic acid,
potassium bromate, potassium iodate or ammonium persulfate) ,
15 another enzyme (e.g. a-amylase, pentosanase or a protease as
explained above), an amino acid (e.g. cysteine) and salt (e.g.
sodium chloride, calcium acetate, sodium sulfate or calcium
sulfate serving to make the dough firmer) .
It is at present contemplated that the exoamylase may be
20 present in the bread improver in an amount of 1-5,000,000 MANU
(as defined above) per kg of the bread improver, preferably 10-
2,500,000 MANU, more preferably 50-1,000,000 MANU, most
preferably 100-500,000 MANU, and in particular 1000-100,000
MANU of the exoamylase per kg of the bread improver. In
25 accordance with conventional practice for the use of bread
improvers, this may be added to flour in an amount of 0.2-10%,
in particular 0.5-5%, by weight of the flour.
The present invention is further illustrated in the following
example which is not in any way intended to limit the scope
30 and spirit of the invention.
WO 91 /04669 PCT/DK90/00244
10
EXAMPLE
White pan bread was prepared from the following ingredients
Wheat flour* 100%
Water 52%
5 Sodium chloride 2%
Baker f s yeast 2.5%
*) commercial wheat flour of moderate
quality (treated with ascorbic acid) :
~ 11% protein, « 15% humidity
10 by mixing with a spiral mixer for 4 minutes at 14 0 rpm and for
3 minutes at 280 rpm (Speed of the spiral rotor) . The dough
temperature was 26 °C. The dough was allowed to rise for 40
minutes at 34 °C and, after degassing and moulding, for 65
minutes at 34 °C. The bread was subsequently baked for 30 mi-
15 nutes at 230 °C.
To the dough ingredients were added varying amounts of
NOVAMYL™ (a recombinant maltogenic amylase encoded by a DNA
sequence derived from Bacillus strain NCIB 11837, described in
US 4,598,048), Fungamyl 1600 S (a commercial ct-amylase
2 0 available from Novo-Nordisk a/s) and Veron F25 (a commercial
a-amylase available from Rohm), respectively. The results ap-
pear from the following tables.
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11
Table 1
NOVAMYL™, 1500 MANU/g
Dosage in g/lOOkg of flour
Properties
Dough
10
Volume
index
Crumb
15 structure
Crumb
freshness
(48 h)
20 Crumb
freshness
(72 h)
Crumb
freshness
25 (96 h)
Gummy
crumb
6.7 13.3 27
53 107
short short short short short short
struc- struc- struc- struc- struc- struc-
ture ture ture ture ture ture
100 99
99
fine fine fine
100 100 101
coarser
100 240 270 280 310 310
100 160 200 230 270 270
100 160 390 425 500 580
no
no
no
no
no yes
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12
Table 2
Fungamyl™ 1600 S
Dosage in g/lOOkg of flour
Properties
Dough
10
10 20 40 80 160
short pos. pos. dough dough dough
struc- too too too
ture soft soft soft
Volume
index
Crumb
structure
15
Crumb
freshness
(48 h)
2 0 Crumb
freshness
(72 h)
Crumb
freshness
25 (96 h)
100 102 107 107 106 106
fine fine/ fine/
ripe ripe
coarser
100 240 280 290 330 320
100 145 240 230 280 290
100 200 250 530 650 675
Gummy
crumb
no no no no/yes yes • yes
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13
Table 3
Veron F25
Dosage in g/lOOkg of flour
Properties
Dough
10 Volume
index
Crumb
structure
Crumb
15 freshness
(48 h)
Crumb
freshness
20 (72 h)
Crumb
freshness
(96 h)
Gummy
25 crumb
10
short pos,
struc-
ture
100
100
20
40
80 106
pos.
100
pos,
102
pos ,
102
fine fine fine
pos,
102
coarser
100 210 210 210 235 210
100 125 125
230
no
no
no no/yes yes yes
It appears from the tables above that, compared to the use of
Fungamyl 1600 S and Veron F25, the addition of NOVAMYL™ to
dough leads to improved storage properties of the resulting
bread without a concomitant gumminess of the crumb which only
30 occurs a far larger dosage of the enzyme. NOVAMYL™ does not
significantly change other dough or bread characteristics.
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14
CLAIMS
1. A process for retarding the staling of leavened baked pro-
ducts comprising adding an enzyme with exoamylase activity to
flour or dough.
5 2. A process according to claim 1, wherein the enzyme with
exoamylase activity is a B-amylase or maltogenic amylase.
3. A process according to claim 1, wherein enzyme is one ex-
hibiting activity at and above the gelation temperature of
starch *
10 4. A process according to claim 1, wherein the enzyme is a
microbial exoamylase .
5 . A process according to claim 2 or 4 , wherein the maltogenic
amylase is one producible by Bacillus strain NCIB 11837, or one
encoded by a DNA sequence derived from Bacillus strain NCIB
15 11837.
6. A process according to claim 5 f wherein the enzyme is added
in an amount of 0.1-10,000 MANU (as defined herein) per kg of
flour.
7. A process according to claim 6, wherein the enzyme is added
20 in an amount of 1-5000 MANU, preferably 5-2000 MANU, and most
preferably 10-1000 MANU, per kg of flour.
8. A process according to claim 1, wherein a suitable yeast
culture is added to the dough.
9. A process according to claim 1, wherein the baked product
25 is white bread, whole-meal bread, or bread produced from mix-
tures of wheat and rye flour.
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15
10. A process according to claim 1, wherein one or more other
enzymes are added to the flour or dough,
11. A process according to claim 10, wherein the other en-
zyme (s) is/are a-amylase, pentosanase or a protease.
5 12. A process according to claim 1, wherein one or more emul-
sifiers are added to the flour or dough.
13. A process according to claim 12 , wherein the emulsif ier (s)
is/are mono- or diglycerides , polyoxyethylene stearates,
diacetyl tartaric acid esters of monoglycer ides , sugar esters
10 of fatty acids, propylene glycol esters of fatty acids,
polyglycerol esters of fatty acids, lactic acid esters of
monoglycerides , acetic acid esters of monoglycer ides , lecithin
or phospholipids.
14. A baked product produced by the process according to any
15 of claims 1-13.
15. An agent for improving the quality of leavened baked pro-
ducts, which agent comprises an enzyme with exoamylase acti-
vity in liquid or substantially dry form.
16. An agent according to claim 15, wherein the enzyme with
2 0 exoamylase activity is a glucoamylase, 6-amylase or maltogenic
amylase.
17. An agent according to claim 15, wherein enzyme is one ex-
hibiting activity at the gelation temperature of starch.
18. An agent according to claim 15 or 16, wherein the enzyme
25 is a microbial exoamylase.
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16
19. An agent according to claim 18 , wherein the maltogenic
amylase is one producible by Bacillus strain NCIB 11837,
or one encoded by a DNA sequence derived from Bacillus strain
NCIB 11837.
5 20. An agent according to any of claims 15-19, which further
comprises one or more components selected from the group con-
sisting of milk powder, gluten, an emulsifier, granulated fat,
an oxidant (e.g. ascorbic acid, potassium bromate, potassium
iodate or ammonium persulfate) , another enzyme (e.g. a-amylase,
10 pentosanase or a protease) , an amino acid (e.g. cystein) and a
salt (e.g. sodium chloride, calcium acetate, sodium sulfate or
calcium sulfate) .
INTERNATIONAL SEARCH REPORT
International Application No PCT/DK 90/00244
I. CLASSIFICATION OF SUBJECT MATTER (if several classification symbols apply, indicate all) 6
According to International Patent Classification (IPC) or to both National Classification and IPC
IPCS: A 21 D 8/04
II. FIELDS SEARCHED
Minimum Documentation Searched
Classification System
Classification Symbols
IPC5
A 21 D
Documentation Searched other than Minimum Documentation
to the Extent that such Documents are Included in Fields Searched 8
SE,DK,FI,N0 classes as above
III. DOCUMENTS CONSIDERED TO BE RELEVANT 9
Category *
Citation of Document, 11 with indication, where appropriate, of the relevant passages 1
Chemical Abstracts, volume 107, no. 5, 3 August
1987, (Columbus, Ohio, US), see page 576, abstra
ct 38380q, & JP,, 6279745 (Okada, Shigetaka et a
1) 1987
Chemical Abstracts, volume 107, no. 5, 3 August
1987, (Columbus, Ohio, US), see page 576, abstra
ct 38381r, & JP, , 6279746 (Okada, Shigetaka et a
1) 1987
EP, A2, 0171995 (KYOWA HAKKO KOGYO CO., LTD.)
19 February 1986,
see pages 2 and 3
Relevant to Claim No. 13
1-4,6-
18,20
5,19
1-4,6-
18,20
5,19
1-3,6-
17,20
4-5,18-
19
* Special categories of cited documents: 10
*A* document defining the general state of the art which is not
considered to be of particular relevance
*E" earlier document but published on or after the international
filing date
"V document which may throw doubts on priority clatm(s} or
which is cited to establish the pubhcation.date of another
citation or other special reason (as specified)
*cr document referring to an oral disclosure, use, exhibition or
other means
"P" document published prior to the international filing date but
later than the priority date claimed
T* later document published after the international filing date
or priority date and not in conflict with the application but
cited to understand the principle or theory underlying the
invention
"X" document of particular relevance, the claimed, invention
cannot be considered novel or cannot be considered to
involve an inventive step
*Y* document of particular relevance, the claimed invention l
cannot be considered to involve an inventive step when the
document is combined with one or more other such docu-
ments, such combination being obvious to a person skilled
in the art.
document member of the same patent family
IV. CERTIFICATION
Date of the Actual Completion of the International Search
19th December 1990
International Searching Authority
SWEDISH PATENT OFFICE
Date of Mailing of this International Search Report
1991 -01- 02
Signature or Authorized Offleen
Kerstin Bolie Janson
Form PCT/iSA/210 (second sheet) (January 1985)
International Application No. PCT/DK 90/00244
111. DOCUMENTS CONSIDERED TO BE RELEVANT (CONTINUED FROM THE SECOND SHEET)
Category ■
Citation of Document, with indication, where appropriate, of the relevant passages
Relevant to Claim No
Y
US, A, 4598048 (DIDERICHSEN ET AL)
1 July 1986, see abstract
5,19
X
Allan Himmel stein 11 Enzyme treatment of flour", 1984,
Bakers Digest, New York,
see Fig 2 and 5
1-4,6-
18,20
X
EP, A2, 0154135 (LI EKEN-BATSCHEIDER MuHLEN- UND
BACKBETRIEBE GMBH) 11 September 1985,
see page 3, 3:rd col.
1-2,8-
16,20
Fom PCT/ISA/Z10 C extra sheet) (January 1985)
ANNEX TO THE INTERNATIONAL SEARCH REPORT
ON INTERNATIONAL PATENT APPLICATION NO.PCT/DK 90/00244
This annex lists the patent family members relating to the patent documents cited in the above-mentioned international search report.
The members are as contained in the Swedish Patent Office EDP file on JJ.tLJl „ f information
The Swedish Patent Office is in no way liable for these particulars which are merely given for the purpose of information.
Patent document
cited in search report
Publication
date
Patent family
member(s)
Publication
date
EP-A2-
0171995
86-02-
■19
CA-A-
JP-A-
JP-A-
1262654
61047133
61056037
89-11-07
86-03-07
86-03-20
US-A-
4598048
86-07-
■01
CA-A-
EP-A-B-
JP-A-
US-A-
1214407
0120693
60002185
4604355
86-11-25
84- 10-03
85- 01-08
86- 08-05
EP-A2-
0154135
85-09-
■11
DE-A-C-
DE-A-
3402778
3437789
85- 08-08
86- 04-17
4
9